ID A0A135TI63_9PEZI Unreviewed; 716 AA.
AC A0A135TI63;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidase family M28 {ECO:0000313|EMBL:KXH47853.1};
GN ORFNames=CNYM01_01371 {ECO:0000313|EMBL:KXH47853.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH47853.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH47853.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH47853.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXH47853.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JEMN01001107; KXH47853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135TI63; -.
DR Proteomes; UP000070054; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08022; M28_PSMA_like; 1.
DR CDD; cd02121; PA_GCPII_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 1.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..716
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007803832"
FT DOMAIN 167..223
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 351..539
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 602..714
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
SQ SEQUENCE 716 AA; 78181 MW; 73CE16F42623FA0A CRC64;
MRQSLLSLAL TVTSVHACQR DWAALNRRIK SHSHHDHGHK KRDMAVEYPP SLTEYESILV
NSFDSKSLDE WSHYYTSGDH LGGHNRTLAE WTQQKWIDAG WDASIEEYWI WYTAPLETTL
SLNRPDGSVH NVSLIEDMLE EDPTTSYPNR IPAYHAMSGS GNISAEYVYV GRGQRGDFQA
LKDAGIELEG KIALSMYGAI YRGTKVKNAQ DNGMIGAVLF TDPLDDGEIT VANGYLAYPA
RNPSMIQRGS VRFSSLYSGD PSTVGYASEK DGPRNDVTPY NPTIPSVPIS MKDAVPLLAA
LDGSGLSAEQ VNRSSWIGAL PNITYSSGPT PGATLDMVHF MNQTVAPSWD VIGIINGTHP
DEVLIIGNHR DAWVIGGAAD PNSGSAVLIE LSKAFGKLLD KGWKPRRTII LGSWDAEEFG
LQGSTEWVES HLPWLVTNAV AYLNLDVAVS GPRTALSGSG EIQTVAIEMM KKVLFPEDWG
VGPTLYDMWF NTTEGEIAPL GSGSDYASFY HNGISAIDIG SDGGKTDPVY HYHGHYDSYT
WMAKFGDPGF KIHRVMGQWL TLIAYHIADD VIIPWDLPNA GRVLRTYYED LNETIAGDYP
SLSLSPIDDA ITEFETAAER IATVAKQALA FNDTVLIDVI NSKYRDFSRG FASAGGLPGR
PTFHNVISAP GLDNGYGADV FPAVQDSLSS GNETQAQEWV EKSASAISRA AEILGI
//